Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase.

Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase.
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DOI:
10.1021/bi9001437
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发表时间:
2009-03-24
期刊:
影响因子:
2.9
通讯作者:
Bandarian, Vahe
Bandarian, Vahe
中科院分区:
生物学3区
文献类型:
--
作者:
McCarty, Reid M.;Somogyi, Arpad;Bandarian, Vahe

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为了阐明含7-脱氮嘌呤的天然产物生物合成过程中所需的早期步骤,我们研究了大肠杆菌QueD催化的反应,QueD是一种可能参与肌苷生物合成的6-乙酰基-5,6,7,8-四氢蝶呤合酶(PTPS)同系物。哺乳动物的PTPS同源物在生物蝶呤的生物合成中将7,8-二氢新蝶呤三磷酸(H2 NTP)转化为6-乙酰四氢蝶呤(PPH 4),而E. coli QueD催化H2 NTP转化为6-羧基-5,6,7,8-四氢蝶呤(CPH4)。E. coli QueD也可以将PPH 4和sepiapterin转化为CPH 4,从而提出了一种机制。
To elucidate the early steps required during biosynthesis of a broad class of 7-deazapurine containing natural products, we have studied the reaction catalyzed by Escherichia coli QueD, a 6-pyruvoyl-5,6,7,8-tetrahydropterin synthase (PTPS) homolog possibly involved in queuosine biosynthesis. While mammalian PTPS homologs convert 7,8-dihydroneopterin triphosphate (H2NTP) to 6-pyruvoyltetrahydropterin (PPH4) in biopterin biosynthesis, E. coli QueD catalyzes the conversion of H2NTP to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4). E. coli QueD can also convert PPH4 and sepiapterin to CPH4, allowing a mechanism to be proposed.
DOI: 10.1073/pnas.0408056102
发表时间: 2005-03-22
影响因子: 11.1
作者:
Van Lanen, SG;Reader, JS;Iwata-Reuyl, D
通讯作者: Iwata-Reuyl, D
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